Agonist stimulation provokes dendritic and axonal dopamine D1 receptor redistribution in primary cultures of striatal neurons

Martin-Negrier, Marie Laure; Charron, G.; Bloch, Bertrand

doi:10.1016/s0306-4522(00)00187-1

Cited by 23 publications

(19 citation statements)

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“…In the same rat primary striatal cell culture, D1R stimulation by the D1R full agonist SKF-82958 induces a dramatic redistribution of D1R immunolabeling corresponding to an internalization of the receptor in early endosomes, as expected and previously reported (Martin-Negrier et al, 2000 (Fig. 6b,d,e).…”

Section: Proteasome Inhibition Dramatically Limits D1r Internalizationsupporting

confidence: 88%

“…Four animals were randomly selected in each group for measuring proteasome catalytic activity. Primary medium spiny neuron culture: Sprague Dawley rat striatal cultures were prepared as previously described (Kowalski and Giraud, 1993;Martin-Negrier et al, 2000;Martin-Negrier et al, 2006). All the reagents for the culture were purchased from Sigma and Invitrogen.…”

Section: Rodent Experimentsmentioning

confidence: 99%

“…In all other conditions, incubation media contained 0.1% of DMSO. For the agonist-induced internalization of D1R, cells were incubated with 10 M of the full D1R agonist SKF-82958 (Martin-Negrier et al, 2000;Martin-Negrier et al, 2006). To test the effect of the inhibition of proteasome activity on D1R trafficking, neurons were incubated with bortezomib for 60 min before 60 min incubation with SKF-82958.…”

Section: Rodent Experimentsmentioning

confidence: 99%

“…At the end of incubation, the medium was rapidly removed and replaced by fixative agent. For proteasomal activity assays, cells cultured for 14 d were incubated at 37°C in a 5% CO 2 incubator with either H 2 O, dopamine (10 M) and acid ascorbic, the full D1R agonist SKF-82958 (10 M) (Martin-Negrier et al, 2000, the D1R antagonist SCH-23390 (2 M), the D2R agonist Quinpirole (10 M) (Brami-Cherrier et al, 2002), or both agonists, diluted in culture medium for 60 min. At the end of incubation, the medium was rapidly removed and cells were rinsed three times with PBS, detached mechanically, and collected.…”

Section: Rodent Experimentsmentioning

confidence: 99%

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l-DOPA Impairs Proteasome Activity in Parkinsonism through D₁Dopamine Receptor

Berthet¹,

Bézard²,

Porras³

et al. 2012

J. Neurosci.

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Aberrant membrane localization of dopamine D 1 receptor (D1R) is associated with L-DOPA-induced dyskinesia (LID), a major complication of L-DOPA treatment in Parkinson's disease (PD). Since the proteasome plays a central role in modulating neuronal response through regulation of neurotransmitter receptor intraneuronal fate, we hypothesized that the ubiquitine-proteasome proteolytic pathway could be impaired in LID. Those LIDs are actually associated with a striatum-specific decrease in proteasome catalytic activity and accumulation of polyubiquitinated proteins in experimental rodent and monkey parkinsonism. We then demonstrated that such decreased proteasome catalytic activity (1) results from D1R activation and (2) feed-back the D1R abnormal trafficking, i.e., its exaggerated cell surface abundance. We further showed that the genetic invalidation of the E3 ubiquitin-protein ligase parkin PD gene leads to exaggerated abnormal involuntary movements compared with wild-type mice. We thus established in an unprecedented series of experimental models that impairment of the ubiquitine-proteasome system at specific nodes (E3 ligase parkin, polyubiquitination, proteasome catalytic activity) leads to the same phenomenon, i.e., aberrant behavioral response to dopamine replacement therapy in PD, highlighting the intimate interplay between dopamine receptor and proteasome activity in a nondegenerative context.

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Section: Proteasome Inhibition Dramatically Limits D1r Internalizationsupporting

confidence: 88%

Section: Rodent Experimentsmentioning

confidence: 99%

Section: Rodent Experimentsmentioning

confidence: 99%

Section: Rodent Experimentsmentioning

confidence: 99%

See 2 more Smart Citations

l-DOPA Impairs Proteasome Activity in Parkinsonism through D₁Dopamine Receptor

Berthet¹,

Bézard²,

Porras³

et al. 2012

J. Neurosci.

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“…Treatment for 2, 5 and 20 min with SKF-82958, an efficacious dopamine D1-like receptor-selective agonist (Martin-Negrier et al 2000), enhanced the colocalization of the D1 receptor with arrestin3 and not arrestin2. Translocation of arrestin3 to the membrane in neurons was confirmed by quantification of arrestin immunoreactivity in membranes prepared from agonisttreated neuronal cultures; the abundance in the membrane of arrestin3, but not arrestin2, was enhanced by D1 receptor activation.…”

Section: Discussionmentioning

confidence: 96%

Dopamine D1 receptor interaction with arrestin3 in neostriatal neurons

Macey

Liu

Gurevich

et al. 2005

Journal of Neurochemistry

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Dopamine D1 receptor interactions with arrestins have been characterized using heterologously expressed D1 receptor and arrestins. The purpose of this study was to investigate the interaction of the endogenous D1 receptor with endogenous arrestin2 and 3 in neostriatal neurons. Endogenous arrestin2 and 3 in striatal homogenates bound to the C-terminus of the D1 receptor in a glutathione-S-transferase (GST) pulldown assay, with arrestin3 binding more strongly. The D1 C-terminus and, to a lesser extent, the third cytoplasmic loop also bound purified arrestin2 and 3. In neostriatal neurons, 2, 5, and 20 min agonist treatment increased the colocalization of the D1 receptor and arrestin3 immunoreactivity without altering the colocalization of the D1 receptor and arrestin2. Further, agonist treatment for 5 and 20 min caused translocation of arrestin3, but not arrestin2, to the membrane. The binding of arrestin3, but not arrestin2, to the D1 receptor was increased as assessed by coimmunoprecipitation after agonist treatment for 5 and 20 min. Agonist treatment of neurons induced D1 receptor internalization (35-45%) that was maximal within 2-5 min, a time-course similar to that of the increase in colocalization of the D1 receptor with arrestin3. These data indicate that the D1 receptor preferentially interacts with arrestin3 in neostriatal neurons. Keywords: arrestin, D1 dopamine receptor, G proteincoupled receptor, receptor internalization. Arrestin plays a critical role in the desensitization of G protein-coupled receptors (GPCRs) by binding to GPCR kinase-phosphorylated receptors, resulting in dissociation of the G protein from the receptor. Arrestin then targets the receptor to clathrin-coated pits for internalization and either degradation or recycling back to the membrane for resensitization (Pippig et al. 1995;Tsao et al. 2001). Arrestin can also promote the stable interaction of signaling proteins with the GPCR (Luttrell et al. 2001).Based on their rates of resensitization and relative affinities for arrestin2 and 3, GPCRs have been classified into two groups, class A and B. Residues within the C-terminal tail of the receptor appear to contribute to the stability of the receptorarrestin complex, which determines the rate of resensitization of the GPCR (Oakley et al. 2000). Class A receptors dissociate from arrestin relatively fast and are rapidly dephosphorylated and recycled back to the membrane. Class A receptors also have a higher affinity for arrestin3 than 2 (Shenoy and Lefkowitz 2003). Class B receptors remain associated with arrestin during internalization, which makes the recycling and dephosphorylation of the receptor occur more slowly, and have a similar affinity for arrestin2 and 3 (Shenoy and Lefkowitz 2003). The dopamine D1 receptor has been designated a class A GPCR, along with the b 2 -adrenoceptor, whereas the neurokinin NK-1 and vasopression V2 receptors are examples of class B GPCRs (Oakley et al. 2000).Desensitization and internalization of the dopamine D1 receptor have been described i...

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Receptor recycling mediates plasma membrane recovery of dopamine D1 receptors in dendrites and axons after agonist‐induced endocytosis in primary cultures of striatal neurons

Martin‐Négrier

Charron

Bloch

2006

Synapse

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The pharmacological stimulation of G-protein-coupled receptor induces receptor internalization. Receptor's fate after the step of internalization remains poorly characterized despite its incidence on the neuronal responsiveness. In this context, we studied the dopamine (DA) D1 receptor (D1R) trafficking in a model of striatal neuronal culture that endogenously express the D1R. We first characterized by immunohistochemistry the spatial distribution of the compartments involved in the endocytic pathways and then the D1R trafficking in dendrites and axons. In dendrites, immunohistochemical analysis showed that acute stimulation by the D1R agonist SKF 82958 (1 microM) induces an internalization of D1R in early endosomes labeled with Alexa-488-conjugated transferrin. We show that, 20 min after removal of the agonist, the D1R immunolabeling pattern returns to the basal state in dendrites and in axons. Recovery was unaffected by cycloheximide (70 microM) but was prevented by monensin (100 microM) that inhibits endosomal acidification and receptor recycling. These data suggest that dendritic and axonal D1Rs are internalized after agonist stimulation and targeted to the recycling pathway demonstrating that the machinery involved in GPCR endocytosis and recycling is functional both in dendrites and in axons. Temporal characteristics observed for the recovery of D1R density to the basal state and those observed for the resensitization process strongly suggest that D1R recycling supports the receptor resensitization.

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Agonist stimulation provokes dendritic and axonal dopamine D1 receptor redistribution in primary cultures of striatal neurons

Cited by 23 publications

References 50 publications

l-DOPA Impairs Proteasome Activity in Parkinsonism through D₁Dopamine Receptor

l-DOPA Impairs Proteasome Activity in Parkinsonism through D₁Dopamine Receptor

Dopamine D1 receptor interaction with arrestin3 in neostriatal neurons

Receptor recycling mediates plasma membrane recovery of dopamine D1 receptors in dendrites and axons after agonist‐induced endocytosis in primary cultures of striatal neurons

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Agonist stimulation provokes dendritic and axonal dopamine D1 receptor redistribution in primary cultures of striatal neurons

Cited by 23 publications

References 50 publications

l-DOPA Impairs Proteasome Activity in Parkinsonism through D1Dopamine Receptor

l-DOPA Impairs Proteasome Activity in Parkinsonism through D1Dopamine Receptor

Dopamine D1 receptor interaction with arrestin3 in neostriatal neurons

Receptor recycling mediates plasma membrane recovery of dopamine D1 receptors in dendrites and axons after agonist‐induced endocytosis in primary cultures of striatal neurons

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l-DOPA Impairs Proteasome Activity in Parkinsonism through D₁Dopamine Receptor

l-DOPA Impairs Proteasome Activity in Parkinsonism through D₁Dopamine Receptor